1-hexylpyridinium and n-octadecyl-mercaptan

Surface-enhanced Raman spectroscopy (SERS) was used to detect different spectral features of small (1-2 nm) and large (5-10 nm) synthetic amyloid Aβ-42 oligomers, exhibiting high and no detectable neurotoxicities, respectively. Adsorption of peptides at self-assembled monolayers (SAM) terminated by methyl and pyridinium groups was employed to differentiate toxic and non-toxic oligomers. Three SAMs were analyzed: hydrophobic heptanethiol (HT) and octadecanethiol (ODT) as well as positively charged N-(6-mercapto)hexylpyridinium (MHP) chloride. SERS study revealed twofold adsorption effect, changes in the monolayer structure and appearance of new bands associated with the adsorbed peptides. A band at 1387 cm(-1), observed as a result of the SAM and Aβ-42 interaction, is tentatively assigned to the peptide symmetric stretching vibration of carboxylate groups, and appears to be the most prominent spectral feature distinguishing toxic oligomers from the non-toxic Aβ-42 forms. This band was identified in the spectra of Aβ-42 adsorption on heptanethiol and MHP monolayers, while no clear perturbations were observed in the case of ODT monolayer.

Topics: Adsorption; Amyloid beta-Peptides; Electrodes; Heptanes; Protein Structure, Quaternary; Pyridinium Compounds; Spectrum Analysis, Raman; Sulfhydryl Compounds; Surface Properties